Observation of tissue prokallikrein activation by some serine proteases, arginine esterases in rat submandibular gland.
Two serine proteases, arginine esterases (esterases I and II) which showed the activity of tissue prokallikrein activation were identified in rat submandibular gland. These enzymes were separated from the homogenate of rat submandibular gland by two successive DEAE-cellulose chromatographies and were further purified and characterized. Esterases I and II were found to be identical with tonin and esterase B-like enzyme, respectively. Both enzymes activated rat urinary prokallikrein at near neutral pH. Esterase B-like enzyme activated rat urinary prokallikrein better than tonin.
Kamada
M
M
Department of Biochemistry, Faculty of Pharmaceutical Sciences, Science University of Tokyo, Japan.
Furuhata
N
N
Yamaguchi
T
T
Ikekita
M
M
Kizuki
K
K
Moriya
H
H
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002265:Carboxylic Ester Hydrolases / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D002848:Chromatography, DEAE-Cellulose / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D007527:Isoenzymes / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism; D007700:Kinetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011288:Prekallikrein / Q000378:metabolism* / Q000652:urine; D011480:Protease Inhibitors / Q000494:pharmacology; D051381:Rats; D012697:Serine Endopeptidases / Q000378:metabolism*; D013363:Submandibular Gland / Q000201:enzymology*
D007527:Isoenzymes; D011480:Protease Inhibitors; D011288:Prekallikrein; C019724:arginine esterase; D002265:Carboxylic Ester Hydrolases; D012697:Serine Endopeptidases